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Q13216 (ERCC8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA excision repair protein ERCC-8
Alternative name(s):
Cockayne syndrome WD repeat protein CSA
Gene names
Name:ERCC8
Synonyms:CKN1, CSA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. Ref.9 Ref.10 Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Interacts with ERCC6 and KIAA1530/UVSSA. Interacts with a subunit of RNA polymerase II TFIIH. Interacts with DDB1. Ref.8 Ref.9 Ref.13

Subcellular location

Nucleus Probable.

Involvement in disease

Cockayne syndrome A (CSA) [MIM:216400]: A rare disorder characterized by cutaneous sensitivity to sunlight, abnormal and slow growth, cachectic dwarfism, progeroid appearance, progressive pigmentary retinopathy and sensorineural deafness. There is delayed neural development and severe progressive neurologic degeneration resulting in mental retardation. Two clinical forms are recognized: in the classical form or Cockayne syndrome type 1, the symptoms are progressive and typically become apparent within the first few years or life; the less common Cockayne syndrome type 2 is characterized by more severe symptoms that manifest prenatally. Cockayne syndrome shows some overlap with certain forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum, patients with Cockayne syndrome do not manifest increased freckling and other pigmentation abnormalities in the skin and have no significant increase in skin cancer.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.14 Ref.15 Ref.17

UV-sensitive syndrome 2 (UVSS2) [MIM:614621]: An autosomal recessive disorder characterized by cutaneous photosensitivity and mild freckling in the absence of neurological abnormalities or skin tumors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Contains 5 WD repeats.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCockayne syndrome
Deafness
Disease mutation
Dwarfism
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 11782547. Source: UniProtKB

nucleotide-excision repair

Inferred from mutant phenotype PubMed 17297471. Source: UniProtKB

positive regulation of DNA repair

Inferred from mutant phenotype Ref.1. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

response to UV

Inferred from direct assay Ref.8. Source: UniProtKB

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from direct assay PubMed 11782547. Source: UniProtKB

transcription-coupled nucleotide-excision repair

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentCul4A-RING E3 ubiquitin ligase complex

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear matrix

Inferred from direct assay PubMed 11782547. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleotide-excision repair complex

Inferred from direct assay Ref.8. Source: MGI

nucleus

Inferred from direct assay PubMed 11782547. Source: MGI

protein complex

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10944529Ref.8Ref.13Ref.1. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERCC6Q034682EBI-596556,EBI-295284
XAB2Q9HCS73EBI-295260,EBI-295232

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13216-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13216-2)

The sequence of this isoform differs from the canonical sequence as follows:
     185-205: HRQEILAVSWSPRYDYILATA → IFILFQTATTLSKRFNKKKRY
     206-396: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396DNA excision repair protein ERCC-8
PRO_0000050970

Regions

Repeat41 – 7232WD 1
Repeat97 – 12832WD 2
Repeat184 – 21532WD 3
Repeat243 – 27331WD 4
Repeat332 – 36231WD 5

Amino acid modifications

Modified residue3901Phosphoserine Ref.12
Modified residue3911Phosphoserine Ref.12
Modified residue3921Phosphoserine Ref.12

Natural variations

Alternative sequence185 – 20521HRQEI…ILATA → IFILFQTATTLSKRFNKKKR Y in isoform 2.
VSP_013914
Alternative sequence206 – 396191Missing in isoform 2.
VSP_013915
Natural variant1501S → C.
Corresponds to variant rs167037 [ dbSNP | Ensembl ].
VAR_053392
Natural variant1601A → T in CSA. Ref.17
Corresponds to variant rs281875222 [ dbSNP | Ensembl ].
VAR_063507
Natural variant1601A → V in CSA. Ref.15
Corresponds to variant rs121434325 [ dbSNP | Ensembl ].
VAR_025380
Natural variant1941W → C in CSA. Ref.17
Corresponds to variant rs281875223 [ dbSNP | Ensembl ].
VAR_063508
Natural variant2001Y → C. Ref.4
Corresponds to variant rs4647105 [ dbSNP | Ensembl ].
VAR_016319
Natural variant2021L → S in CSA. Ref.17
Corresponds to variant rs281875224 [ dbSNP | Ensembl ].
VAR_063509
Natural variant2051A → P in CSA. Ref.14
Corresponds to variant rs121434326 [ dbSNP | Ensembl ].
VAR_025381
Natural variant2661D → G in CSA. Ref.17
Corresponds to variant rs281875225 [ dbSNP | Ensembl ].
VAR_063510
Natural variant3611W → C in UVSS2. Ref.16
Corresponds to variant rs281875221 [ dbSNP | Ensembl ].
VAR_068177

Secondary structure

....................................................................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EC962D56226D717B

FASTA39644,055
        10         20         30         40         50         60 
MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML 

        70         80         90        100        110        120 
SGGSDGVIVL YDLENSSRQS YYTCKAVCSI GRDHPDVHRY SVETVQWYPH DTGMFTSSSF 

       130        140        150        160        170        180 
DKTLKVWDTN TLQTADVFNF EETVYSHHMS PVSTKHCLVA VGTRGPKVQL CDLKSGSCSH 

       190        200        210        220        230        240 
ILQGHRQEIL AVSWSPRYDY ILATASADSR VKLWDVRRAS GCLITLDQHN GKKSQAVESA 

       250        260        270        280        290        300 
NTAHNGKVNG LCFTSDGLHL LTVGTDNRMR LWNSSNGENT LVNYGKVCNN SKKGLKFTVS 

       310        320        330        340        350        360 
CGCSSEFVFV PYGSTIAVYT VYSGEQITML KGHYKTVDCC VFQSNFQELY SGSRDCNILA 

       370        380        390 
WVPSLYEPVP DDDETTTKSQ LNPAFEDAWS SSDEEG 

« Hide

Isoform 2 [UniParc].

Checksum: 6553CE607A392576
Show »

FASTA20523,182

References

« Hide 'large scale' references
[1]"The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH."
Henning K.A., Li L., Iyer N., McDaniel L.D., Reagan M.S., Legerski R., Schultz R.A., Stefanini M., Lehmann A.R., Mayne L.V., Friedberg E.C.
Cell 82:555-564(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-200.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Urinary bladder.
[8]"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDB1, IDENTIFICATION IN THE CSA COMPLEX WITH RBX1; DDB1 AND CUL4A, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9 SIGNALOSOME.
[9]"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome."
Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y.
Genes Dev. 20:1429-1434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERCC6, FUNCTION AS SUBSTRATE-RECOGNITION COMPONENT OF THE CSA COMPLEX.
[10]"Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo."
Fousteri M., Vermeulen W., van Zeeland A.A., Mullenders L.H.
Mol. Cell 23:471-482(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-391 AND SER-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair."
Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.
Nat. Genet. 44:593-597(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UVSSA.
[14]"CKN1 (MIM 216400): mutations in Cockayne syndrome type A and a new common polymorphism."
Cao H., Williams C., Carter M., Hegele R.A.
J. Hum. Genet. 49:61-63(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CSA PRO-205.
[15]"Characterisation of novel mutations in Cockayne syndrome type A and xeroderma pigmentosum group C subjects."
Ridley A.J., Colley J., Wynford-Thomas D., Jones C.J.
J. Hum. Genet. 50:151-154(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CSA VAL-160.
[16]"A UV-sensitive syndrome patient with a specific CSA mutation reveals separable roles for CSA in response to UV and oxidative DNA damage."
Nardo T., Oneda R., Spivak G., Vaz B., Mortier L., Thomas P., Orioli D., Laugel V., Stary A., Hanawalt P.C., Sarasin A., Stefanini M.
Proc. Natl. Acad. Sci. U.S.A. 106:6209-6214(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT UVSS2 CYS-361.
[17]"Mutation update for the CSB/ERCC6 and CSA/ERCC8 genes involved in Cockayne syndrome."
Laugel V., Dalloz C., Durand M., Sauvanaud F., Kristensen U., Vincent M.C., Pasquier L., Odent S., Cormier-Daire V., Gener B., Tobias E.S., Tolmie J.L., Martin-Coignard D., Drouin-Garraud V., Heron D., Journel H., Raffo E., Vigneron J. expand/collapse author list , Lyonnet S., Murday V., Gubser-Mercati D., Funalot B., Brueton L., Sanchez Del Pozo J., Munoz E., Gennery A.R., Salih M., Noruzinia M., Prescott K., Ramos L., Stark Z., Fieggen K., Chabrol B., Sarda P., Edery P., Bloch-Zupan A., Fawcett H., Pham D., Egly J.M., Lehmann A.R., Sarasin A., Dollfus H.
Hum. Mutat. 31:113-126(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSA THR-160; CYS-194; SER-202 AND GLY-266.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28413 mRNA. Translation: AAA82605.1.
CR536563 mRNA. Translation: CAG38800.1.
BT020021 mRNA. Translation: AAV38824.1.
AY213194 Genomic DNA. Translation: AAO21128.1.
AK314511 mRNA. Translation: BAG37111.1.
CH471123 Genomic DNA. Translation: EAW55004.1.
BC009793 mRNA. Translation: AAH09793.1.
CCDSCCDS3978.1. [Q13216-1]
PIRA57090.
RefSeqNP_000073.1. NM_000082.3. [Q13216-1]
NP_001007235.1. NM_001007234.2. [Q13216-2]
UniGeneHs.435237.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A11X-ray3.31B1-396[»]
ProteinModelPortalQ13216.
SMRQ13216. Positions 1-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107581. 35 interactions.
DIPDIP-291N.
IntActQ13216. 9 interactions.
MINTMINT-1417899.
STRING9606.ENSP00000265038.

PTM databases

PhosphoSiteQ13216.

Polymorphism databases

DMDM3121917.

Proteomic databases

MaxQBQ13216.
PaxDbQ13216.
PRIDEQ13216.

Protocols and materials databases

DNASU1161.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265038; ENSP00000265038; ENSG00000049167. [Q13216-1]
GeneID1161.
KEGGhsa:1161.
UCSCuc003jsl.3. human. [Q13216-1]
uc003jsn.3. human. [Q13216-2]

Organism-specific databases

CTD1161.
GeneCardsGC05M060169.
GeneReviewsERCC8.
H-InvDBHIX0004887.
HGNCHGNC:3439. ERCC8.
MIM216400. phenotype.
609412. gene.
614621. phenotype.
neXtProtNX_Q13216.
Orphanet90321. Cockayne syndrome type 1.
90322. Cockayne syndrome type 2.
90324. Cockayne syndrome type 3.
178338. UV-sensitive syndrome.
PharmGKBPA27853.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000248233.
HOVERGENHBG005409.
InParanoidQ13216.
KOK10570.
OMAQELYSGG.
PhylomeDBQ13216.
TreeFamTF101237.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SignaLinkQ13216.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13216.
BgeeQ13216.
CleanExHS_ERCC8.
GenevestigatorQ13216.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiERCC8_(gene).
GenomeRNAi1161.
NextBio4822.
PROQ13216.
SOURCESearch...

Entry information

Entry nameERCC8_HUMAN
AccessionPrimary (citable) accession number: Q13216
Secondary accession number(s): B2RB64, Q6FHX5, Q96GB9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM